Through centuries of evolution, nature has developed  biomacromolecules capable of folding and assembling into discrete structures with a functional consequence.  Specifically, protein biosynthetic and evolutionary pathways are key processes that can be explored to develop functional macromolecules with precise structure.  This in combination with the chemist's ability to produce diversity beyond the building blocks of nature, offers a powerful tool for the design and synthesis of new functional macromolecules.  In particular, we have sought to integrate fluorinated amino acid analogs in order to: (1) reprogram stability and function within enzymes and (2) fabricate protein materials with controlled assemblies and mechanical properties.  Our studies demonstrate the significant effects of fluorination with potential applications in biocatalysis and medicine.

Fluorinating proteins: From enhanced stability to modulating mechanical properties

245th National Meeting (2013)

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